Strong skin, not always thick: Comparative structural and molecular analysis of deer skin and cow hide

Abstract

Content: A comprehensive analysis of the molecular and structural components of deer skin and cow hide was undertaken. These skins known to be strong, however they derive their strength from different combinations of molecular and structural properties. Firstly, the physical properties of deer skin and cow hide including the tensile strength, tear strength and denaturation temperature were measured. Secondly, the structure of the collagen fibrils and glycosaminoglycans was investigated using transmission electron microscopy (TEM), and small angle X-ray scattering (SAXS). Finally, the chemical composition of deer skin and cow hide such as amino acids, crosslinks and glycosaminoglycans were analysed. Our results showed that physical properties of deer skin and cow hide are derived from different combinations of several chemical components resulting in different architecture. It was found that the large and “wavy” collagen fibres in deer skin made up of collagen fibrils with small diameters. Additionally, deer skin fibrils appeared to be linked by regular arrays of filaments of large glycosaminoglycans that are distributed uniformly. Deer skin contained higher proportion of trivalent collagen crosslinks. In contrast, the collagen fibrils in cow hide were large, contained a diverse glycosaminoglycan distribution and a higher proportion of tetravalent collagen crosslinks, resulting in straight collagen fibres. This study suggests that although deer skin and cow hide are both strong, they have different structural and molecular features. Take-Away: Deer skin and cow hide have different structural and molecular make up which are reflected in their physical properties particularly strength. Glycosaminoglycans are important for the organisation of collagen fibrils in deer skin and cow hide. Deer skin and cow hide contain different ratios of collagen natural crosslinks which are essential collagen stability